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bacteria:t3e:xopaj [2020/09/29 22:21]
lindsay.triplett_ct.gov 		bacteria:t3e:xopaj [2022/06/22 13:56]
rkoebnik
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 Authors: [[https://www.researchgate.net/profile/Ralf_Koebnik|Ralf Koebnik]] & Trainees from the 2<sup>nd</sup>  EuroXanth Training School ([[https://www.researchgate.net/profile/Daiva_Burokiene|Daiva Burokienė]], [[https://www.researchgate.net/profile/ermic_Edyta|Edyta Đermić]], [[https://www.researchgate.net/profile/Dagmar_Stehlikova|Dagmar Stehlikova]], [[https://www.researchgate.net/profile/Mariya_Stoyanova|Mariya Stoyanova]])\\ Authors: [[https://www.researchgate.net/profile/Ralf_Koebnik|Ralf Koebnik]] & Trainees from the 2<sup>nd</sup>  EuroXanth Training School ([[https://www.researchgate.net/profile/Daiva_Burokiene|Daiva Burokienė]], [[https://www.researchgate.net/profile/ermic_Edyta|Edyta Đermić]], [[https://www.researchgate.net/profile/Dagmar_Stehlikova|Dagmar Stehlikova]], [[https://www.researchgate.net/profile/Mariya_Stoyanova|Mariya Stoyanova]])\\
 Internal reviewer: [[https://www.researchgate.net/profile/Joel_Pothier2|Joël F. Pothier]]\\ Internal reviewer: [[https://www.researchgate.net/profile/Joel_Pothier2|Joël F. Pothier]]\\
-Expert reviewer: Lindsay Triplett+Expert reviewer: [[https://www.researchgate.net/profile/Lindsay_Triplett|Lindsay Triplett]]
  
 Class: XopAJ\\ Class: XopAJ\\
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   * AvrRxo1 is a kinase that converts NAD to 3'-NADP and NAADP to 3'-NAADP. Mutation of the catalytic aspartic acid residue D<sub>193</sub>  abolished AvrRxo1 kinase activity and several phenotypes of AvrRxo1, including toxicity in yeast, bacteria, and plants, suppression of the flg22-triggered ROS burst, and ability to trigger an //R//  gene-mediated hypersensitive response in rice. A mutation in the Walker A ATP-binding motif, which reduced 3'-NADP production by roughly 90%, abolished the toxicity of AvrRxo1 in bacteria, yeast, and plants. However, this mutation did not abolish the virulence enhancement, ROS suppression, or HR-triggering phenotypes of AvrRxo1. These results demonstrate that AvrRxo1 kinase activity is required for all the known phenotypes of AvrRxo1, but that toxicity is dose-dependent (Shidore //et al.//, 2017).   * AvrRxo1 is a kinase that converts NAD to 3'-NADP and NAADP to 3'-NAADP. Mutation of the catalytic aspartic acid residue D<sub>193</sub>  abolished AvrRxo1 kinase activity and several phenotypes of AvrRxo1, including toxicity in yeast, bacteria, and plants, suppression of the flg22-triggered ROS burst, and ability to trigger an //R//  gene-mediated hypersensitive response in rice. A mutation in the Walker A ATP-binding motif, which reduced 3'-NADP production by roughly 90%, abolished the toxicity of AvrRxo1 in bacteria, yeast, and plants. However, this mutation did not abolish the virulence enhancement, ROS suppression, or HR-triggering phenotypes of AvrRxo1. These results demonstrate that AvrRxo1 kinase activity is required for all the known phenotypes of AvrRxo1, but that toxicity is dose-dependent (Shidore //et al.//, 2017).
   * AvrRxo1 targets the cysteine protease RD21A, which is required for drought-induced immunity (Liu //et al.//, 2020).   * AvrRxo1 targets the cysteine protease RD21A, which is required for drought-induced immunity (Liu //et al.//, 2020).
 +  * AvrRxo1 enhances //Xoc//  virulence and inhibits stomatal immunity by targeting and degrading rice OsPDX1 (pyridoxal phosphate synthase), thereby reducing vitamin B6 (VB6) levels in rice (Liu //et al.//, 2022).
  
 === Localization === === Localization ===
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 === Enzymatic function === === Enzymatic function ===
  
-AvrRxo1 has a T4 polynucleotide kinase domain (Han //et al.//, 2015; Wu //et al//., 2015).+AvrRxo1 has a T4 polynucleotide kinase domain (Han //et al.//, 2015; Wu //et al//., 2015). AvrRxo1 is an ATP-dependent protease (Liu //et al.//, 2022).
  
 AvrRxo1 is a phosphotransferase that produces two novel metabolites by phosphorylating nicotinamide/nicotinic acid adenine dinucleotide at the adenosine 3'-hydroxyl group. Both products of AvrRxo1, 3'-NADP and 3'-nicotinic acid adenine dinucleotide phosphate (3'-NAADP), had been used before as inhibitors or signaling molecules but were regarded as "artificial" compounds until then (Schuebel //et al.//, 2016). AvrRxo1 has weak phosphorylation activity on some other nucleotides including ATP (Scheubel //et al. //2016) AvrRxo1 is a phosphotransferase that produces two novel metabolites by phosphorylating nicotinamide/nicotinic acid adenine dinucleotide at the adenosine 3'-hydroxyl group. Both products of AvrRxo1, 3'-NADP and 3'-nicotinic acid adenine dinucleotide phosphate (3'-NAADP), had been used before as inhibitors or signaling molecules but were regarded as "artificial" compounds until then (Schuebel //et al.//, 2016). AvrRxo1 has weak phosphorylation activity on some other nucleotides including ATP (Scheubel //et al. //2016)
  
-AvrRxo1 phosphorylates NAD //in planta//, and its kinase catalytic sites are necessary for toxicity, suppression of PAMP-triggered immunity, and activation of Rxo1-mediated resistance (Shidore //et al.//, 2017). In a metabolomic profile, 3'-NADP accumulated upon expression of AvrRxo1 in //E. coli//, yeast, //N. benthamiana//  and in rice leaves infected with //avrRxo1//-expressing strains of //X. oryzae//, suggesting that the AvrRxo1 product is not utilized or degraded by the cell (Shidore //et al.//, 2017). 3'-NADP was the only metabolite observed to accumulate in an //avrRxo1//-dependent manner, and it is not known whether NAADP is phosphorylated by AvrRxo1 //in planta // (Shidore //et al.//, 2017).+AvrRxo1 phosphorylates NAD //in planta//, and its kinase catalytic sites are necessary for toxicity, suppression of PAMP-triggered immunity, and activation of Rxo1-mediated resistance (Shidore //et al.//, 2017). In a metabolomic profile, 3'-NADP accumulated upon expression of AvrRxo1 in //E. coli//, yeast, //N. benthamiana//  and in rice leaves infected with //avrRxo1//-expressing strains of //X. oryzae//, suggesting that the AvrRxo1 product is not utilized or degraded by the cell (Shidore //et al.//, 2017). 3'-NADP was the only metabolite observed to accumulate in an //avrRxo1//-dependent manner, and it is not known whether NAADP is phosphorylated by AvrRxo1 //in planta //  (Shidore //et al.//, 2017).
  
 === Interaction partners === === Interaction partners ===
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 Yes (//Acidovorax//  spp., //Paraburkholderia andropogonis//) (Triplett //et al.//, 2016). Yes (//Acidovorax//  spp., //Paraburkholderia andropogonis//) (Triplett //et al.//, 2016).
  
-Homologs of the //avrRxo1:arc1//  operon in which the avrRxo1 homolog lacks a type III secretion signal are found in other environmental microbes, including the filamentous myxobacteria //Cystobacter fuscus//  and uncultured candidate //Saccharimonas//  and //Parcubacteria// spp. (Triplett// et al.//  2016).+Homologs of the //avrRxo1:arc1//  operon in which the avrRxo1 homolog lacks a type III secretion signal are found in other environmental microbes, including the filamentous myxobacteria //Cystobacter fuscus//  and uncultured candidate //Saccharimonas//  and //Parcubacteria//  spp. (Triplett// et al.//  2016).
  
 ===== References ===== ===== References =====

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